Tubulin GTPase
| Tubulin GTPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.6.5.6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Tubulin GTPase (EC 3.6.5.6) is an enzyme with systematic name GTP phosphohydrolase (microtubule-releasing).[1][2][3] This enzyme catalyses the following chemical reaction
- GTP + H2O GDP + phosphate
This enzyme participates in tubulin folding and division plane formation.
See also
References
- ↑ Yu, X.C.; Margolin, W. (1997). "Ca2+-mediated GTP-dependent dynamic assembly of bacterial cell division protein FtsZ into asters and polymer networks in vitro". EMBO J. 16: 5455–5463. PMC 1170176
. PMID 9312004. doi:10.1093/emboj/16.17.5455. - ↑ Tian, G.; Bhamidipati, A.; Cowan, N.J.; Lewis, S.A. (1999). "Tubulin folding cofactors as GTPase-activating proteins. GTP hydrolysis and the assembly of the α/β-tubulin heterodimer". J. Biol. Chem. 274: 24054–24058. PMID 10446175. doi:10.1074/jbc.274.34.24054.
- ↑ Roychowdhury, S.; Panda, D.; Wilson, L.; Rasenick, M.M. (1999). "G protein α subunits activate tubulin GTPase and modulate microtubule polymerization dynamics". J. Biol. Chem. 274: 13485–13490. PMID 10224115. doi:10.1074/jbc.274.19.13485.
External links
- Tubulin GTPase at the US National Library of Medicine Medical Subject Headings (MeSH)
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